Isolation of a mannose-binding and IgE- and IgM-reactive lectin from the seeds of Artocarpus integer.
A mannose-binding lectin, termed champedak lectin-M, was isolated from an extract of the crude seeds of champedak (Artocarpus integer). On gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kDa. SDS-PAGE showed the mannose-binding lectin to be composed of 16.8 kDa polypeptides with some of the polypeptides being disulphide-linked to give dimers. When tested with all isotypes of immunoglobulins, champedak lectin-M demonstrated a selective strong interaction with human IgE and IgM, and a weak interaction with IgA2. The binding interactions of lectin-M were metal ion independent. The lectin was also shown to interact with horseradish peroxidase, ovalbumin, porcine thyroglobulin, human alpha1-acid glycoprotein, transferrin and alpha1-antitrypsin. It demonstrated a binding preference to Man alpha 1-3Man ligands in comparison to Man alpha 1-6Man or Man alpha 1-2Man.
Lim
S B
SB
Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur, Malaysia.
Chua
C T
CT
Hashim
O H
OH
D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D037222:Collectins; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D007073:Immunoglobulin E / Q000378:metabolism*; D007075:Immunoglobulin M / Q000378:metabolism*; D007477:Ions; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D008670:Metals; D037121:Plant Lectins; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants; D012639:Seeds
D002352:Carrier Proteins; D037222:Collectins; D006023:Glycoproteins; D007075:Immunoglobulin M; D007477:Ions; D037102:Lectins; D008670:Metals; D037121:Plant Lectins; D010940:Plant Proteins; D007073:Immunoglobulin E